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A4WN07 (SYA_PYRAR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine--tRNA ligase

EC=6.1.1.7
Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS
Gene names
Name:alaS
Ordered Locus Names:Pars_2228
OrganismPyrobaculum arsenaticum (strain DSM 13514 / JCM 11321) [Complete proteome] [HAMAP]
Taxonomic identifier340102 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length892 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain By similarity. HAMAP MF_00036_A

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_A

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_A

Subcellular location

Cytoplasm By similarity HAMAP MF_00036_A.

Domain

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs By similarity. HAMAP MF_00036_A

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

alanine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 892892Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000347890

Sites

Metal binding5941Zinc By similarity
Metal binding5981Zinc By similarity
Metal binding7021Zinc By similarity
Metal binding7061Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A4WN07 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 7EB632860ED831CA

FASTA89299,831
        10         20         30         40         50         60 
MLSAKILERS GYLRKQCPLC KSYFWTLRHD QVYCGDQPCV PYGFIGSPPV KVAVDSLTEL 

        70         80         90        100        110        120 
RERFLRFFER RGHARIKRYP VVARWRDDVY LVGASIYDFQ PWVTSGAVPP PANPLVISQP 

       130        140        150        160        170        180 
SIRLTDVDKV GRSGRHLTGF EMMAHHAFNY PDKYVYWIDE TTEYAYEFFT KELGITPEEI 

       190        200        210        220        230        240 
TFKESMWEGG GNAGECYEVL VRGLEVATLV FMHYETKEGK YVELPLKIVD TGYGLERIYW 

       250        260        270        280        290        300 
LLKGTPTIYD AVFGPFLDRA RQKLGVPEPP AEVMGKASIY FGQMDPEVIG LEKAYDLIAE 

       310        320        330        340        350        360 
KIGVDGKWLR EVFRPQEALY VLADHSRTVS WMIADGVIPS NSGAGYLARL LIRRILKNLK 

       370        380        390        400        410        420 
LAGIEAPLVE LIDMHLKELK VDYPEVWAAR DLILELVDLE ERKYKEILKS APTVVKKALD 

       430        440        450        460        470        480 
EARRRGAASL SPDDLVALYD SFGLPPEIVA DVAKTQGVEV KVPDDFYSRL AARHAKKEKQ 

       490        500        510        520        530        540 
PESTLVEMAK VIDLPRTREL FYEDPYMRSF KAKVLRVVDG KYVVLDQTAF YAEGGGQPGD 

       550        560        570        580        590        600 
VGVLKYSGGA AKVVDVQRVG HIIVHVVEGQ PPPEGVEVVG EIDWERRYAL MKMHTGTHVL 

       610        620        630        640        650        660 
IQSIRRVLGP HIWQAGAQKD IPSSRLDVTH YKLPTPEEVA EIERLANSAV QANLPVYVKI 

       670        680        690        700        710        720 
MPRNEAEAKY GFILYQGGVV PAREIRVVQI GPDSDPYDVQ ACGGTHLKST GEIGIIKIQK 

       730        740        750        760        770        780 
VERIADGVVR FIFTTGLHAL SYIQELERQL GQAAQVAGGS RDNVVEAVKR LASRAEEAER 

       790        800        810        820        830        840 
KWRHYAELYA KQMAQSLKAE QVGRYKLAVV ELDDEDLAKK VAEEATGRDK DLVLVVMGGN 

       850        860        870        880        890 
KLSIFTGGAD VAPIVKSLRE VGFRGGGSRT FAQGVYSGDV KTLIDALRRA LS 

« Hide

References

[1]"Complete sequence of Pyrobaculum arsenaticum DSM 13514."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13514 / JCM 11321.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000660 Genomic DNA. Translation: ABP51774.1.
RefSeqYP_001154426.1. NC_009376.1.

3D structure databases

ProteinModelPortalA4WN07.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4WN07.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5056335.
GenomeReviewsGene locus Pars_2228 in contig CP000660_GR.
KEGGpas:Pars_2228.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBA4WN07.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycPARS340102:PARS_2228-MONOMER.

Family and domain databases

HAMAPMF_00036_A. Ala_tRNA_synth_A.
[Tree]
InterProIPR002318. Ala-tRNA-synth_IIc.
IPR018162. Ala-tRNA-synth_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR022429. Ala-tRNA_synth_arc.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMsTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_PYRAR
AccessionPrimary (citable) accession number: A4WN07
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families